The dynamics of protein folding have long been of interest. However, the timescales on which key folding events occur have been inaccessible using standard liquid NMR and other biochemical techniques. Solid state deuterium NMR is sensitive to motions on the order of 101 - 1010 sec-1 and thus is ideal for studying molecular dynamics. The recent discovery of a class of short peptides which readily form helices in water provides a model system which can be studied using deuterium NMR to determine rates and activation energies of folding. Before determining the rates, a clearer understanding of the structures formed is necessary. Thus, we have undertaken measuring key distances in the helices formed to determine whether alpha helices or 310 helices are formed. Specifically, we have been measuring homonuclear and heteronuclear dipolar couplings using the solid state NMR techniques R2 and REDOR.